ID M7AG15_CHEMY Unreviewed; 1467 AA.
AC M7AG15;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Caskin-2 {ECO:0000313|EMBL:EMP23801.1};
DE Flags: Fragment;
GN ORFNames=UY3_19243 {ECO:0000313|EMBL:EMP23801.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP23801.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB608654; EMP23801.1; -; Genomic_DNA.
DR STRING; 8469.M7AG15; -.
DR eggNOG; KOG0507; Eukaryota.
DR eggNOG; KOG4384; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR CDD; cd09497; SAM_caskin1_2_repeat1; 1.
DR CDD; cd09498; SAM_caskin1_2_repeat2; 1.
DR CDD; cd12063; SH3_Caskin2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2.
DR InterPro; IPR033635; ANKS1/Caskin.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR032232; Caskin1-CID.
DR InterPro; IPR035497; Caskin1/2_SAM_1.
DR InterPro; IPR035498; Caskin1/2_SAM_2.
DR InterPro; IPR035499; Caskin2_SH3.
DR InterPro; IPR032117; Caskin_C.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR24174:SF18; CASKIN-2; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF16907; Caskin-Pro-rich; 1.
DR Pfam; PF16632; Caskin-tail; 1.
DR Pfam; PF16600; Caskin1-CID; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00454; SAM; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1467
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004079551"
FT REPEAT 1..31
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 32..64
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 65..97
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 139..171
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 171..203
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 232..298
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 457..520
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 526..590
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 314..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP23801.1"
SQ SEQUENCE 1467 AA; 158550 MW; BA605E63088A5F59 CRC64;
FSALHHAALG GSLELISLLL EAQATVDIKD SNGMRPLHYA AWQGRVEPVH LLLRAAASVN
MASLDGQIPL HLSAQYGHYE VSEMLLQHQS NPCLINKAKK TPLDLACEFG RLKVAQLLLN
SHMCVALLEG QSKDTSDPNY TTPLHLAAKN GHKEIIRQLL KAGIEINRQT KTGTALHEAA
LYGKTEVVRL LLEGGVDVNI RNTYNQTALD IVNQFTTSHA SKDIKQLLRE ASGILKVRAL
KDFWNLHDPT ALNIRAGDII TVLEQHSDGR WKGHIHDTQK GTDRVGYFPP SIVEVISKRT
GMTLPRLVPA HQRQGIAAPP GGLQPLPGDA PQQAPLSLPT AYGHLTLTRT APEPENSAGD
RNSVGSEGSI GSIRSAGSGQ STEGNNGQST SILIENATPL PPGGEDLQLH LLGSNSQNGQ
LNSLTGTLGR QNLTNCNASN RIFSHQYLRP EQLLEGKDAE AIYNWLSEFQ LEFYTANFLN
AGYDVPTISR MTPEDLTAIG VTKPGHRKKI STEIGQLSIA EWLPNYIPAD LMEWLSAIGL
PQYHKKLVSN GYDSISIVTD LTWEDLQEIG INKLGHQKKI MLAVKKLTDI RKNLNQADTK
LARRKIPGAL DIVTIESVEN GESQSPHTPK MITFQDSELS YELQTAMSNS CQETLPMKNT
QGMSRSQESI GVRSRGSGHS QDNMLSKTIL SSHSQESLGS GSSSSGHSST QPRQKENADV
LPGRPNQDNY GKVITKLTTQ EGLNGYSNGC GGSPLKERNL PEGTDQYQRP VAQKGSVPLL
QPSNSLPAAT PCTPLQTPNK GTAPYVFMYP HISLKSPGVP EQPKNPAHLY PQFSSTPRSN
LQSSAQKAFS YLHSHCSGTE SPYMSPKPGA TLGSWQAGEQ QNGDTFKYKK RSHSLNRKTR
YARSDGEHEK EEGVTSTLGS YATLTRRPGR SQVPRTYLQS DSKVVRSQSF AIRAKRKGPP
PPPPKRLSSV SSAQAMEAEG EQGLESERRP AVAQDSVDVA PSPWLGTSNA GTSQTVKSIA
AMLEVPTVGG SPPKPLLLQK PPTPDHELVS RAGSDGQPCG ARISEGSCSM RLSDNERDAF
GNNRPRRRTF SEPSVTTMEA LQSSLEDVQS DTEEERRPGP EDCEISSLSS QNSSSECIPF
AEEGNLTIKQ RPKPTGQHKA EATSRDSESS SPTAADVGPP CSSAGKELGG TTEKELEVLE
FNLTESDTVK RRPRCKEREP LQTLLKVFSL AGQSQALASP PPQYAQAQAV SIMGPALQVP
EPRGNGDSFD DDRVEFRIAE IEKSILSLEK GVKKPPLSLK SASPGELHEG AVRLRTSPVG
PDASAKHTSV ASTKLVFSGP KTIYQQVLQP SRNTIAPWAT AEMAPEVAGS TAVACPSKLE
IGNKAVLSSG MPIFMKPLSA APDAALAQQR LEQTNSSLAA ALQAAEKKIT AEELDSHYGA
THSANNILED ISNMFDDLAD QLDAMLD
//
